Physical Principles and Techniques of Protein ChemistryPhysical Principles and Techniques of Protein Chemistry Part C ... |
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Page 127
10 , A6292 for titration of both the carboxyl and amino groups is positive ( low pH
reference solution ) , but A€263 is negative . At 243 mu , an absorption change is
observed only for the titration of the carboxyl group , since this wavelength is an ...
10 , A6292 for titration of both the carboxyl and amino groups is positive ( low pH
reference solution ) , but A€263 is negative . At 243 mu , an absorption change is
observed only for the titration of the carboxyl group , since this wavelength is an ...
Page 145
8 ) , the wavelength of maximum slope for these solvent - exposed ( normal )
phenolic groups is 286 . 0 – 0 . ... This may be considered the normal spectral
shift resulting from covalent attachment of a phenolic group to a protein , at its
surface .
8 ) , the wavelength of maximum slope for these solvent - exposed ( normal )
phenolic groups is 286 . 0 – 0 . ... This may be considered the normal spectral
shift resulting from covalent attachment of a phenolic group to a protein , at its
surface .
Page 146
Sydney J. Leach. JF . REPORTER GROUPS Although most proteins contain a
large number of chromophores , it may be that none of these chromophores is
located in or near a region which is important to the biological function of the
protein .
Sydney J. Leach. JF . REPORTER GROUPS Although most proteins contain a
large number of chromophores , it may be that none of these chromophores is
located in or near a region which is important to the biological function of the
protein .
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Contents
The Enhancement of Contrast | 21 |
The Preservation of Specimens | 35 |
Examples of the Application of Electron Microscopy to the Study | 48 |
Copyright | |
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Common terms and phrases
absorbance absorption acid appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores complex concentration constant containing contrast corrected corresponding curve decrease dependence determined dielectric difference diffusion dipole direction discussed distribution effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor fluorescence fraction frequency function given groups Herskovits important increase indicates intensity interactions ionic ions length light limited macromolecules measured method mobility molecular molecules observed obtained occurs optical orientation particles patterns peaks perturbation phase phenolic polarization position possible preparation present produced protein quantum range ratio reaction reference relative relaxation respectively rotation sample separation serum albumin shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion transfer transition tryptophan unit usually volume wavelength yield zone